Electrophoretic analysis of Antarctic fish from South Georgia

White muscle samples of Antarctic fish ( Notothenia rossii, N., neglecta. N. gibbe-rifrons and Chaenocephalus (aceratus ) were subjected to electrophoretic tests. lsoelectric focusing of general muscle proteins provides a quick method of iden-tyfying species. Six muscle enzymes were resolved by horizontal starch gel clectrophoresis. These are presumed to be the products of ten independent gene loci. Coefficients of genetic distance were calculated and substantially agree with the conventional taxnomy. Levels of genetic variability are within the normal range for marine teleosts. Two polymorphic enzymes. GPI and PGM. might prove useful as 'genetic tags' for stock identification.     

Functional significance of Micraspis discolor (F.) (Coccinellidae: Coleoptera) in rice ecosystem

Coccinellids are key predators that are conserved and augmented in agricultural ecosystems, to achieve biological control of pests. Actual quantification of field predation has not been attempted for many of the beneficial coccinellids. Numerous reports show coccinellids as opportunistic, feeding on a variety of food material in addition to their preferred prey. Micraspis discolor is the most abundant species of coccinellid in rice ecosystems and touted as a biocontrol option for brown planthopper (BPH), Nilaparvata lugens (Stal), a key pest of rice. However, it has been reported as both entomophagous and phytophagous. Native polyacrylamide gel electrophoresis (PAGE) was used to separate esterases from whole‐body homogenates of Micraspis and its prey viz., green leafhopper (GLH) Nephotettix virescens (Distant), BPH N. lugens, whitebacked planthopper (WBPH) Sogatella furcifera (Horvath), aphid Rhopalosiphum padi L., thrips, Haplothrips sp., and pollen. Field‐collected beetles showed a range of bands, some corresponding with pollen and GLH, while others were different from prey offered, indicating a wider range of prey spectrum than envisaged. Feeding preference studies confirmed a preference for pollen and GLH in no‐choice (H = 20.724; P = 0.001) and multiple‐choice tests (H = 20.52; P < 0.001) and a significant preference for pollen over all insects offered in the paired‐choice test (t = 5.099; P = 0.007). The abundance of adult M. discolor in rice at flowering phase does not correspond to prey abundance in the field but rather reflects an inclination to pollen feeding more than entomophagy.     

Comparaisons des séquences d'ADN hautement répétées chez l'homme et diverses espèces de primates

Highly repeated DNA sequences from man, five other primate species and rat were compared using five restriction endonucleases. Calculations of a similarity index based on the mobility of various bands indicate that man, chimpanzee and baboons are very similar. The sequences of the genomes studied have apparently been reorganized during primate evolution.     

ITPase Activity in Dry Blood Spots is Comparable with That in Fresh Erythrocytes

Inosine triphosphate pyrophosphohydrolase (ITPase) catalyzing the pyrophosphohydrolysis of inosine triphosphate, deoxyinosine triphosphate and xanthosine triphosphate is involved in the metabolism and tolerance of thiopurine drugs. ITPase activity plays an important role in the prediction of toxicity to thiopurine therapy. Activities in dry blood spots were compared with fresh erythrocytes. Samples were incubated with inosine triphosphate, then inosine monophosphate was determined by a capillary electrophoresis method. Calculated enzyme activities obtained from dry blood spots were in good accordance with activity in fresh erythrocytes.     

Identification of Putative Biomarkers for Toluene-Degrading Burkholderia and Pseudomonads by Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry and Peptide Mass Fingerprinting

The use of peptide mass fingerprinting with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) was demonstrated to identify and phenotypically characterize toluene-degrading bacteria via biomarkers of degradation and taxonomical classification. Pseudomonas putida F1, P. mendocina KR1, and Burkholderia sp. JS150 were grown on toluene, extracted, electrophoretically separated, and analyzed by MALDI-TOF MS. Catabolic enzymes were identified and results substantiated using tandem MS.     

An electrophoretic approach to Basidiomycetes taxonomy: Intraspecific variability,varieties, ecological influences

Abstract

Basidiospores of several Basidiomycetes species were treated with electrophoretic techniques, comparing the different protein fractions of the soluble component of the spores wall. The electrophoretic data were elaborated to obtain dendrograms indicating the similarity degree. The method was set up and tested for its validity. The technique showed that the degree of variability within the observed species escaped any generalization, covering a broad range; it was possible to identify the varieties in dendrograms of species grown in the same/different geographical zones; the growing environment and the symbiotic host often influenced the electrophoretic pattern of the spore wall proteins and resulted in dendrograms reflecting the ecological conditions.

Abbreviations: ACP, acid phosphatases; EST, esterases; UPGMA, unweighed pair‐group method using arithmetical average     

Electrophoretic types of leucine aminopeptidase in sheep serum

Leucine aminopeptidase in sheep serum was studied by starch gel electrophoresis. Two phenotypes, A and B, were observed, of which the former was present in 70–90 % of all the sheep examined. These two phenotypes have been shown to be controlled by a single autosomal locus, with two alleles Lay^A and Lap^B . The Lap^A allele is dominant. The frequencies of Lap phenotypes and alleles were determined in eleven Spanish and two foreign breeds. Serum alkaline phospatase and serum leucine aminopeptidase are electrophoretically distinct.     

Increased production of low molecular weight recombinant proteins in Escherichia coli.

A general method for obtaining high-level production of low molecular weight proteins in Escherichia coli is described. This method is based on the use of a novel Met-Xaa-protein construction which is formed by insertion of a single amino acid residue (preferably Arginine or Lysine) between the N-terminal methionine and the protein of interest. The utility of this method is illustrated by examples for achieving high-level production of human insulin-like growth factor-1, human proinsulin, and their analogs. Furthermore, highly produced insulin-like growth factor-1 derivatives and human proinsulin analogs are converted to their natural sequences by removal of dipeptides with cathepsin C.